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Glycan structure analysis

TABLE 6.4 Enzymes commonly used in glycan structure analysis... [Pg.157]

Figure 10.3 Whole-mass analysis of a monoclonal antibody. (A) Direct infusion of the antibody generates an envelope of high m/z ions ranging from 2000 to 3500. Deconvolution of the ion current signal gives the mass of the complete native molecule (147, 100.97 Da) and resolves some heterogeneity linked to the A-glycan structures. The major forms are consistent with molecules carrying biantennary structures capped with 0, 1, or 2 hexose (G = galactose) residues. (Data generated on an ESI-Q-Star instrument, Sciex-Applied Biosystems.)... Figure 10.3 Whole-mass analysis of a monoclonal antibody. (A) Direct infusion of the antibody generates an envelope of high m/z ions ranging from 2000 to 3500. Deconvolution of the ion current signal gives the mass of the complete native molecule (147, 100.97 Da) and resolves some heterogeneity linked to the A-glycan structures. The major forms are consistent with molecules carrying biantennary structures capped with 0, 1, or 2 hexose (G = galactose) residues. (Data generated on an ESI-Q-Star instrument, Sciex-Applied Biosystems.)...
Figure 10.6 Peptide mapping of PIXY321. (A) Cleavage of the primary sequence with Lys-C endoprotease results in 14 theoretical fragments. (B) As detailed in the text, LC-MS analysis of the Lys-C digest shows that a few peptides, notably LI, L7, and L14, elute at several retention times due to heterogeneity of both their glycan structures and amino acid sequence. The insets illustrate the complexity of the mass spectra of glycopeptide LI eluting under peaks 17 (inset C) and 18 (inset D). Figure 10.6 Peptide mapping of PIXY321. (A) Cleavage of the primary sequence with Lys-C endoprotease results in 14 theoretical fragments. (B) As detailed in the text, LC-MS analysis of the Lys-C digest shows that a few peptides, notably LI, L7, and L14, elute at several retention times due to heterogeneity of both their glycan structures and amino acid sequence. The insets illustrate the complexity of the mass spectra of glycopeptide LI eluting under peaks 17 (inset C) and 18 (inset D).
S. F. Wheeler and D. J. Harvey, Extension of the in-gel release method for structural analysis of neutral and sialylated A-linked glycans to the analysis of sulfated glycans Application to the glycans from bovine thyroid-stimulating hormone, Anal. Biochem., 296 (2001) 92-100. [Pg.128]

Viseux, N., de Hoffmann, E. and Domon, B. (1996) An integrated methodology for structural analysis of glycans based on methylation and tandem mass. Glycobiology, 6 (7), 121. [Pg.400]

See other pages where Glycan structure analysis is mentioned: [Pg.176]    [Pg.674]    [Pg.419]    [Pg.421]    [Pg.176]    [Pg.674]    [Pg.419]    [Pg.421]    [Pg.338]    [Pg.514]    [Pg.301]    [Pg.305]    [Pg.6]    [Pg.12]    [Pg.243]    [Pg.276]    [Pg.361]    [Pg.242]    [Pg.252]    [Pg.255]    [Pg.611]    [Pg.118]    [Pg.108]    [Pg.150]    [Pg.197]    [Pg.115]    [Pg.121]    [Pg.121]    [Pg.122]    [Pg.460]    [Pg.89]    [Pg.384]    [Pg.327]    [Pg.227]    [Pg.228]    [Pg.231]    [Pg.234]    [Pg.261]    [Pg.50]    [Pg.596]    [Pg.740]    [Pg.742]    [Pg.745]    [Pg.747]    [Pg.65]    [Pg.1746]    [Pg.1748]    [Pg.1881]    [Pg.2116]   
See also in sourсe #XX -- [ Pg.674 ]



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